ID   CCL7_HUMLU              Reviewed;         544 AA.
AC   M4IRL6;
DT   02-JUN-2021, integrated into UniProtKB/Swiss-Prot.
DT   29-MAY-2013, sequence version 1.
DT   03-AUG-2022, entry version 19.
DE   RecName: Full=Probable CoA ligase CCL7 {ECO:0000305|PubMed:23300257};
DE            Short=HlCCL7 {ECO:0000303|PubMed:23300257};
DE            EC=6.2.1.- {ECO:0000305|PubMed:23300257};
GN   Name=CCL7 {ECO:0000303|PubMed:23300257};
OS   Humulus lupulus (European hop).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   rosids; fabids; Rosales; Cannabaceae; Humulus.
OX   NCBI_TaxID=3486;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], TISSUE SPECIFICITY, DEVELOPMENTAL STAGE, GENE
RP   FAMILY, AND NOMENCLATURE.
RC   STRAIN=cv. Nugget;
RX   PubMed=23300257; DOI=10.1093/mp/sst004;
RA   Xu H., Zhang F., Liu B., Huhman D.V., Sumner L.W., Dixon R.A., Wang G.;
RT   "Characterization of the formation of branched short-chain fatty acid:CoAs
RT   for bitter acid biosynthesis in hop glandular trichomes.";
RL   Mol. Plant 6:1301-1317(2013).
CC   -!- SUBCELLULAR LOCATION: Cytoplasm, cytosol
CC       {ECO:0000250|UniProtKB:M4IRL4}.
CC   -!- TISSUE SPECIFICITY: Mostly expressed at low levels in glandular
CC       trichomes (lupulin glands) after flowering and in flowers, and, to a
CC       lower extent, in stems, leaves and cones.
CC       {ECO:0000269|PubMed:23300257}.
CC   -!- DEVELOPMENTAL STAGE: Accumulates progressively in glandular trichomes
CC       (lupulin glands) after flowering. {ECO:0000269|PubMed:23300257}.
CC   -!- DOMAIN: Both substrate-binding domains (SBD1 and SBD2) are involved in
CC       the substrate recognition, and are sufficient to confer the substrate
CC       specificity. {ECO:0000250|UniProtKB:Q42524}.
CC   -!- SIMILARITY: Belongs to the ATP-dependent AMP-binding enzyme family.
CC       {ECO:0000305}.
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DR   EMBL; JQ740209; AGA17924.1; -; mRNA.
DR   AlphaFoldDB; M4IRL6; -.
DR   SMR; M4IRL6; -.
DR   GO; GO:0005829; C:cytosol; ISS:UniProtKB.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0016405; F:CoA-ligase activity; ISS:UniProtKB.
DR   Gene3D; 3.30.300.30; -; 1.
DR   Gene3D; 3.40.50.12780; -; 1.
DR   InterPro; IPR025110; AMP-bd_C.
DR   InterPro; IPR045851; AMP-bd_C_sf.
DR   InterPro; IPR020845; AMP-binding_CS.
DR   InterPro; IPR000873; AMP-dep_Synth/Lig.
DR   InterPro; IPR042099; ANL_N_sf.
DR   Pfam; PF00501; AMP-binding; 1.
DR   Pfam; PF13193; AMP-binding_C; 1.
DR   PROSITE; PS00455; AMP_BINDING; 1.
PE   2: Evidence at transcript level;
KW   ATP-binding; Cytoplasm; Ligase; Nucleotide-binding.
FT   CHAIN           1..544
FT                   /note="Probable CoA ligase CCL7"
FT                   /id="PRO_0000452952"
FT   REGION          269..338
FT                   /note="SBD1"
FT                   /evidence="ECO:0000250|UniProtKB:Q42524"
FT   REGION          339..403
FT                   /note="SBD2"
FT                   /evidence="ECO:0000250|UniProtKB:Q42524"
FT   BINDING         198..206
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000250|UniProtKB:Q81G39"
FT   BINDING         338..343
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000250|UniProtKB:Q81G39"
FT   BINDING         424
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000250|UniProtKB:Q81G39"
FT   BINDING         436..439
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000250|UniProtKB:Q81G39"
FT   BINDING         530
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000250|UniProtKB:Q81G39"
SQ   SEQUENCE   544 AA;  59534 MW;  C48351DCD437C615 CRC64;
     MEKSGYGRDG VFRSLRPPLV LPKDHNLSMV SFVFRNSSSY PQKPALIDSD TNETLSFSQF
     KSMVIKVSHG FLNLGVQKND VVLIFAPNSI HVPVCFLGIV ASGAIATTSN PLYTVSELSK
     QVKDSNPKLI VTVPELFEKV KGFNLPTILI GPNSEDSSPL KSRAKVLTFH DLVTLSGPVS
     DFPMVDFKQS DTAALLYSSG TTGMSKGVVL SHKNFIASSL MVTMEQDQAG EMHNVFLCFL
     PMFHVFGLAI ITYAQLQRGN TVISMARFDL EKILKDVEKY KVTHLWVVPP VILALTKNSI
     VKKYDLSSLK HIGSGAAPLG KDLMEECAKI VPHGIVAQGY GMTETCGIVS VEDTRGGKRH
     TGSAGMLSSG VEAQIVSVDT LKPLPPNQLG EIWVRGPNMM QGYFNNPRAT KLTIDKKGWV
     HTGDLGYFDE DGHLYVVDRI KELIKYKGFQ VAPAELEGLL VSHPEILDAV VIPFPDADAG
     EVPVAYVVRS PNSSLTEDDV KKFIAGQVAS FKRLRKVTFI NSVPKSASGK ILRRELIQKV
     RSNI